Title

Author

Date Approved

Degree Type

Open Access Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

Committee Member

Deborah Heyl-Clegg, PhD, Chair

Committee Member

Dr. Hedeel Evans, PhD

Committee Member

Dr. Maria Milletti, PhD

Abstract

Human islet amyloid polypeptide protein (hIAPP) is secreted by the pancreas along with insulin and is assumed to play a role in pathological development of type II diabetes. It has 37 amino acids in its sequence. Amyloid is formed due to misfolding of the protein, which is cytotoxic to beta cells in the pancreas of type II diabetic patients. The presence of amyloid deposits is also a characteristic feature of a number of other diseases like Alzheimer’s disease and Parkinson’s disease. Since insulin has been reported to interact with hIAPP and block amyloid formation, fragments of insulin were synthesized and the inhibitory effects were studied against an hIAPP analog in the presence of phospholipid vesicles. While these sequences might inhibit amyloid formation, preliminary results indicate that they actually enhance membrane damage, as measured by the increased leakage of carboxyfluoroscein dye from membrane model vesicles.